Evidence map›Paper›PMID 28103007›Full record

ArticleBiochemistry2017

Glutamate 350 Plays an Essential Role in Conformational Gating of Long-Range Radical Transport in Escherichia coli Class Ia Ribonucleotide Reductase.

Kanchana Ravichandran, Ellen C Minnihan, Qinghui Lin, Kenichi Yokoyama, Alexander T Taguchi, Jimin Shao, Daniel G Nocera, JoAnne Stubbe

Abstract read
In one paragraph

Article in Biochemistry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
1.2field-weighted citation impact, top 23% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

14 citing papers in PubMed, 22 citations in OpenAlex.

  1. 2.6-Å resolution cryo-EM structure of a class Ia ribonucleotide reductase trapped with mechanism-based inhibitor NProceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  2. Article
  3. Review
  4. Journal of the American Chemical Society · 2022
    Article
  5. Article
  6. Article
  7. Article
  8. Conformational Motions and Water Networks at the α/β Interface inJournal of the American Chemical Society · 2020
    Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Glutamate 52-β at the α/β subunit interface ofThe Journal of biological chemistry · 2017
    Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

8 authors at 2 institutions in 2 countries.

Kanchana RavichandranORCID 0000-0001-5050-9719
Ellen C Minnihan
Qinghui LinDepartment of Pathology and Pathophysiology, Key Laboratory of Disease Proteomics of Zhejiang Province, Research Center for Air Pollution and Health, Zhejiang University School of Medicine , Hangzhou 310058, China.
Kenichi Yokoyama
Alexander T Taguchi
Jimin ShaoDepartment of Pathology and Pathophysiology, Key Laboratory of Disease Proteomics of Zhejiang Province, Research Center for Air Pollution and Health, Zhejiang University School of Medicine , Hangzhou 310058, China.
Daniel G NoceraDepartment of Chemistry and Chemical Biology, Harvard University , 12 Oxford Street, Cambridge, Massachusetts 02138, United States.ORCID 0000-0001-5055-320X
Zhejiang University · CNHarvard University · US

Funding

Structure-Function Studies of Ribonucleotide ReductaseR01GM047274 · NIGMS · MICHIGAN STATE UNIVERSITY · PI DANIEL G. NOCERA · 1992 to 2026
$9.9M
Ribonucleotide Reductase: Structure and FunctionR01GM029595 · NIGMS · UNIVERSITY OF WISCONSIN MADISON · PI STUBBE, JOANNE · 1985 to 2016
$6.9M
NIGMS NIH HHS R01 GM029595NIGMS NIH HHS R01 GM047274
6 · The paper itself

Abstract

Escherichia coli class Ia ribonucleotide reductase (RNR) is composed of two subunits that form an active α2β2 complex. The nucleoside diphosphate substrates (NDP) are reduced in α2, 35 Å from the essential diferric-tyrosyl radical (Y

Indexed as

Models, MolecularAdenosine TriphosphateAmino Acid SubstitutionApoenzymesBinding, CompetitiveBiocatalysisCytidine DiphosphateElectron Spin Resonance SpectroscopyElectron TransportEscherichia coli ProteinsFree RadicalsGlutamic AcidHydrogen-Ion ConcentrationKineticsMutagenesis, Site-DirectedMutation3,5-difluorotyrosineAdenosine TriphosphateApoenzymesCytidine DiphosphateEscherichia coli ProteinsFree RadicalsGlutamic AcidNrdB protein, E coliRecombinant ProteinsRibonucleotide ReductasesTyrosine

Identifiers

PMID28103007
PMCPMC5689411
OpenAlexW2578051543

What OpenQuestion holds

Textmetadata
LicenceTDM
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.